RILP_HUMAN
ID RILP_HUMAN Reviewed; 401 AA.
AC Q96NA2; B2RBQ8; Q71RE6; Q9BSL3; Q9BYS3;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Rab-interacting lysosomal protein;
GN Name=RILP; ORFNames=PP10141;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN LATE ENDOCYTOSIS,
RP INTERACTION WITH RAB7A, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=11179213; DOI=10.1093/emboj/20.4.683;
RA Cantalupo G., Alifano P., Roberti V., Bruni C.B., Bucci C.;
RT "Rab-interacting lysosomal protein (RILP): the Rab7 effector required for
RT transport to lysosomes.";
RL EMBO J. 20:683-693(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-81.
RC TISSUE=Kidney, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RA Frigimelica E., Lanfranchi G.;
RT "Study of 100 skeletal muscle full length mRNA (Telethon project B41).";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lung, Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11520070; DOI=10.1006/bbrc.2001.5466;
RA Bucci C., De Gregorio L., Bruni C.B.;
RT "Expression analysis and chromosomal assignment of PRA1 and RILP genes.";
RL Biochem. Biophys. Res. Commun. 286:815-819(2001).
RN [7]
RP FUNCTION IN DYNEIN-DYNACTIN COMPLEX RECRUITMENT.
RX PubMed=11696325; DOI=10.1016/s0960-9822(01)00531-0;
RA Jordens I., Fernandez-Borja M., Marsman M., Dusseljee S., Janssen L.,
RA Calafat J., Janssen H., Wubbolts R., Neefjes J.;
RT "The Rab7 effector protein RILP controls lysosomal transport by inducing
RT the recruitment of dynein-dynactin motors.";
RL Curr. Biol. 11:1680-1685(2001).
RN [8]
RP INTERACTION WITH RAB34.
RX PubMed=12475955; DOI=10.1091/mbc.e02-05-0280;
RA Wang T., Hong W.;
RT "Interorganellar regulation of lysosome positioning by the Golgi apparatus
RT through Rab34 interaction with Rab-interacting lysosomal protein.";
RL Mol. Biol. Cell 13:4317-4332(2002).
RN [9]
RP FUNCTION IN PHAGOSOME MIGRATION AND PHAGOLYSOSOMAL FUSION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12944476; DOI=10.1128/mcb.23.18.6494-6506.2003;
RA Harrison R.E., Bucci C., Vieira O.V., Schroer T.A., Grinstein S.;
RT "Phagosomes fuse with late endosomes and/or lysosomes by extension of
RT membrane protrusions along microtubules: role of Rab7 and RILP.";
RL Mol. Cell. Biol. 23:6494-6506(2003).
RN [10]
RP FUNCTION IN LYSOSOMAL MORPHOLOGY AND DISTRIBUTION, INTERACTION WITH RAB7A
RP AND RAB34, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14668488; DOI=10.1091/mbc.e03-06-0413;
RA Wang T., Wong K.K., Hong W.;
RT "A unique region of RILP distinguishes it from its related proteins in its
RT regulation of lysosomal morphology and interaction with Rab7 and Rab34.";
RL Mol. Biol. Cell 15:815-826(2004).
RN [11]
RP SUBUNIT.
RX PubMed=15996637; DOI=10.1016/j.bbrc.2005.06.067;
RA Colucci A.M.R., Campana M.C., Bellopede M., Bucci C.;
RT "The Rab-interacting lysosomal protein, a Rab7 and Rab34 effector, is
RT capable of self-interaction.";
RL Biochem. Biophys. Res. Commun. 334:128-133(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-315, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP INTERACTION WITH CLN3.
RX PubMed=22261744; DOI=10.1007/s00018-011-0913-1;
RA Uusi-Rauva K., Kyttala A., van der Kant R., Vesa J., Tanhuanpaa K.,
RA Neefjes J., Olkkonen V.M., Jalanko A.;
RT "Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins
RT and modifies location of late endosomal compartments.";
RL Cell. Mol. Life Sci. 69:2075-2089(2012).
RN [14]
RP INTERACTION WITH RAB7A.
RX PubMed=22431521; DOI=10.1128/mcb.06726-11;
RA Mamo A., Jules F., Dumaresq-Doiron K., Costantino S., Lefrancois S.;
RT "The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal
RT sorting.";
RL Mol. Cell. Biol. 32:1855-1866(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-308, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP FUNCTION, AND INTERACTION WITH RAB34 AND FLCN.
RX PubMed=27113757; DOI=10.15252/embr.201541382;
RA Starling G.P., Yip Y.Y., Sanger A., Morton P.E., Eden E.R., Dodding M.P.;
RT "Folliculin directs the formation of a Rab34-RILP complex to control the
RT nutrient-dependent dynamic distribution of lysosomes.";
RL EMBO Rep. 17:823-841(2016).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 244-308 IN COMPLEX WITH RAB7A,
RP SUBUNIT, AND MUTAGENESIS OF PHE-248; ILE-251; LEU-252; ARG-255; LEU-258;
RP LYS-304; MET-305 AND LEU-306.
RX PubMed=15933719; DOI=10.1038/sj.emboj.7600643;
RA Wu M., Wang T., Loh E., Hong W., Song H.;
RT "Structural basis for recruitment of RILP by small GTPase Rab7.";
RL EMBO J. 24:1491-1501(2005).
CC -!- FUNCTION: Rab effector playing a role in late endocytic transport to
CC degradative compartments (PubMed:11696325, PubMed:14668488,
CC PubMed:27113757, PubMed:11179213, PubMed:12944476). Involved in the
CC regulation of lysosomal morphology and distribution (PubMed:14668488,
CC PubMed:27113757). Induces recruitment of dynein-dynactin motor
CC complexes to Rab7A-containing late endosome and lysosome compartments
CC (PubMed:11179213, PubMed:11696325). Promotes centripetal migration of
CC phagosomes and the fusion of phagosomes with the late endosomes and
CC lysosomes (PubMed:12944476). {ECO:0000269|PubMed:11179213,
CC ECO:0000269|PubMed:11696325, ECO:0000269|PubMed:12944476,
CC ECO:0000269|PubMed:14668488, ECO:0000269|PubMed:27113757}.
CC -!- SUBUNIT: Homodimer (PubMed:15996637, PubMed:15933719). Interacts with
CC RAB7A (PubMed:11179213, PubMed:14668488, PubMed:22431521). Interacts
CC with RAB34 (PubMed:14668488, PubMed:12475955, PubMed:27113757).
CC Identified in a complex with MREG and DCTN1; interacts directly with
CC MREG (By similarity). Interacts with CLN3 (PubMed:22261744). Interacts
CC with FLCN; the interaction is direct and promotes association between
CC RILP and RAB34 (PubMed:27113757). {ECO:0000250|UniProtKB:Q5ND29,
CC ECO:0000269|PubMed:11179213, ECO:0000269|PubMed:12475955,
CC ECO:0000269|PubMed:14668488, ECO:0000269|PubMed:15933719,
CC ECO:0000269|PubMed:15996637, ECO:0000269|PubMed:22261744,
CC ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:27113757}.
CC -!- INTERACTION:
CC Q96NA2; P51149: RAB7A; NbExp=8; IntAct=EBI-2856119, EBI-1056089;
CC Q96NA2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2856119, EBI-5235340;
CC Q96NA2; P37173: TGFBR2; NbExp=3; IntAct=EBI-2856119, EBI-296151;
CC Q96NA2; P49754: VPS41; NbExp=4; IntAct=EBI-2856119, EBI-2130459;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:11179213, ECO:0000269|PubMed:12944476}. Lysosome
CC membrane {ECO:0000269|PubMed:11179213, ECO:0000269|PubMed:12944476,
CC ECO:0000269|PubMed:14668488}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000269|PubMed:12944476}. Note=Associated with late endosomal,
CC lysosomal and phagosomal membranes. The interaction with RAB7A is
CC necessary for its recruitment to phagosomes.
CC {ECO:0000269|PubMed:12944476}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96NA2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96NA2-2; Sequence=VSP_016043, VSP_016044;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in fetal heart,
CC heart, stomach, spleen, adrenal gland, thyroid gland, salivary gland,
CC fetal liver, liver and lung. Poorly expressed in brain.
CC {ECO:0000269|PubMed:11179213, ECO:0000269|PubMed:11520070,
CC ECO:0000269|PubMed:14668488}.
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DR EMBL; AJ404317; CAC33443.1; -; mRNA.
DR EMBL; AK055755; BAB71003.1; -; mRNA.
DR EMBL; AK314767; BAG37305.1; -; mRNA.
DR EMBL; AF370391; AAQ15227.1; -; mRNA.
DR EMBL; AJ278711; CAC82174.1; -; mRNA.
DR EMBL; BC004961; AAH04961.1; -; mRNA.
DR EMBL; BC031621; AAH31621.1; -; mRNA.
DR CCDS; CCDS11009.1; -. [Q96NA2-1]
DR RefSeq; NP_113618.2; NM_031430.2. [Q96NA2-1]
DR PDB; 1YHN; X-ray; 3.00 A; B=244-308.
DR PDBsum; 1YHN; -.
DR AlphaFoldDB; Q96NA2; -.
DR SMR; Q96NA2; -.
DR BioGRID; 123679; 52.
DR DIP; DIP-29458N; -.
DR IntAct; Q96NA2; 14.
DR STRING; 9606.ENSP00000301336; -.
DR iPTMnet; Q96NA2; -.
DR PhosphoSitePlus; Q96NA2; -.
DR BioMuta; RILP; -.
DR DMDM; 74732524; -.
DR EPD; Q96NA2; -.
DR jPOST; Q96NA2; -.
DR MassIVE; Q96NA2; -.
DR MaxQB; Q96NA2; -.
DR PaxDb; Q96NA2; -.
DR PeptideAtlas; Q96NA2; -.
DR PRIDE; Q96NA2; -.
DR ProteomicsDB; 77494; -. [Q96NA2-1]
DR ProteomicsDB; 77495; -. [Q96NA2-2]
DR Antibodypedia; 42527; 80 antibodies from 25 providers.
DR DNASU; 83547; -.
DR Ensembl; ENST00000301336.7; ENSP00000301336.6; ENSG00000167705.12. [Q96NA2-1]
DR Ensembl; ENST00000622136.2; ENSP00000481849.1; ENSG00000274145.2. [Q96NA2-1]
DR GeneID; 83547; -.
DR KEGG; hsa:83547; -.
DR MANE-Select; ENST00000301336.7; ENSP00000301336.6; NM_031430.3; NP_113618.2.
DR UCSC; uc002ftd.4; human. [Q96NA2-1]
DR CTD; 83547; -.
DR DisGeNET; 83547; -.
DR GeneCards; RILP; -.
DR HGNC; HGNC:30266; RILP.
DR HPA; ENSG00000167705; Tissue enhanced (heart muscle, skeletal muscle).
DR MIM; 607848; gene.
DR neXtProt; NX_Q96NA2; -.
DR OpenTargets; ENSG00000167705; -.
DR PharmGKB; PA134915969; -.
DR VEuPathDB; HostDB:ENSG00000167705; -.
DR eggNOG; ENOG502RXH1; Eukaryota.
DR GeneTree; ENSGT00940000161117; -.
DR HOGENOM; CLU_044133_1_0_1; -.
DR InParanoid; Q96NA2; -.
DR OMA; KAGQCSF; -.
DR OrthoDB; 890179at2759; -.
DR PhylomeDB; Q96NA2; -.
DR TreeFam; TF313489; -.
DR PathwayCommons; Q96NA2; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR SignaLink; Q96NA2; -.
DR BioGRID-ORCS; 83547; 53 hits in 1073 CRISPR screens.
DR ChiTaRS; RILP; human.
DR EvolutionaryTrace; Q96NA2; -.
DR GeneWiki; RILP_(gene); -.
DR GenomeRNAi; 83547; -.
DR Pharos; Q96NA2; Tbio.
DR PRO; PR:Q96NA2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96NA2; protein.
DR Bgee; ENSG00000167705; Expressed in apex of heart and 94 other tissues.
DR ExpressionAtlas; Q96NA2; baseline and differential.
DR Genevisible; Q96NA2; HS.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IDA:BHF-UCL.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IPI:FlyBase.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IPI:BHF-UCL.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:BHF-UCL.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IDA:UniProtKB.
DR GO; GO:0070676; P:intralumenal vesicle formation; IMP:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; NAS:UniProtKB.
DR GO; GO:0010796; P:regulation of multivesicular body size; IDA:UniProtKB.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR021563; RILP_dimer.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR Pfam; PF11461; RILP; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasmic vesicle;
KW Endosome; Lysosome; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..401
FT /note="Rab-interacting lysosomal protein"
FT /id="PRO_0000097339"
FT DOMAIN 11..101
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 240..316
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 167..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..333
FT /note="Necessary for interaction with RAB7A and RAB34,
FT lysosomal distribution and morphology"
FT REGION 304..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 75..181
FT /evidence="ECO:0000255"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..210
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_016043"
FT VAR_SEQ 211..213
FT /note="WAT -> MGA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_016044"
FT VARIANT 81
FT /note="A -> T (in dbSNP:rs9909321)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_051321"
FT VARIANT 281
FT /note="R -> Q (in dbSNP:rs34982553)"
FT /id="VAR_034417"
FT MUTAGEN 248
FT /note="F->A: Strongly reduces dimerization and localization
FT to late endosomal/lysosomal compartments."
FT /evidence="ECO:0000269|PubMed:15933719"
FT MUTAGEN 251
FT /note="I->A: Abolishes dimerization, interaction with RAB7A
FT and localization to late endosomal/lysosomal compartments."
FT /evidence="ECO:0000269|PubMed:15933719"
FT MUTAGEN 252
FT /note="L->A: Abolishes interaction with RAB7A and
FT localization to late endosomal/lysosomal compartments."
FT /evidence="ECO:0000269|PubMed:15933719"
FT MUTAGEN 255
FT /note="R->A: Abolishes dimerization, interaction with RAB7A
FT and localization to late endosomal/lysosomal compartments."
FT /evidence="ECO:0000269|PubMed:15933719"
FT MUTAGEN 258
FT /note="L->A: Reduces dimerization, interaction with RAB7A
FT and localization to late endosomal/lysosomal compartments."
FT /evidence="ECO:0000269|PubMed:15933719"
FT MUTAGEN 304
FT /note="K->A: Abolishes interaction with RAB7A and
FT localization to late endosomal/lysosomal compartments."
FT /evidence="ECO:0000269|PubMed:15933719"
FT MUTAGEN 305
FT /note="M->A: Abolishes interaction with RAB7A and
FT localization to late endosomal/lysosomal compartments."
FT /evidence="ECO:0000269|PubMed:15933719"
FT MUTAGEN 306
FT /note="L->A: Abolishes interaction with RAB7A and
FT localization to late endosomal/lysosomal compartments."
FT /evidence="ECO:0000269|PubMed:15933719"
FT CONFLICT 284
FT /note="G -> S (in Ref. 1; CAC33443)"
FT /evidence="ECO:0000305"
FT HELIX 248..276
FT /evidence="ECO:0007829|PDB:1YHN"
FT HELIX 284..306
FT /evidence="ECO:0007829|PDB:1YHN"
SQ SEQUENCE 401 AA; 44200 MW; 1057A1DAC2FFED94 CRC64;
MEPRRAAPGV PGWGSREAAG SASAAELVYH LAGALGTELQ DLARRFGPEA AAGLVPLVVR
ALELLEQAAV GPAPDSLQVS AQPAEQELRR LREENERLRR ELRAGPQEER ALLRQLKEVT
DRQRDELRAH NRDLRQRGQE TEALQEQLQR LLLVNAELRH KLAAMQTQLR AAQDRERERQ
QPGEAATPQA KERARGQAGR PGHQHGQEPE WATAGAGAPG NPEDPAEAAQ QLGRPSEAGQ
CRFSREEFEQ ILQERNELKA KVFLLKEELA YFQRELLTDH RVPGLLLEAM KVAVRKQRKK
IKAKMLGTPE EAESSEDEAG PWILLSDDKG DHPPPPESKI QSFFGLWYRG KAESSEDETS
SPAPSKLGGE EEAQPQSPAP DPPCSALHEH LCLGASAAPE A
